Caspase-cleaved tau exhibits rapid memory impairment associated with tau oligomers in a transgenic mouse model

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works

Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein

Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371 · see citing works

Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice

Chapman, P. F., White, G. L., Jones, M. W., Cooper-Blacketer, D., Marshall, V. J., Irizarry, M., Younkin, L., Good, M. A., Bliss, T. V. P., Hyman, B. T., et al. (1999) · Nature Neuroscience · doi:10.1038/6374 · Cited by 946 · see citing works

Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau

Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works

Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543 · see citing works

Fighting neurodegeneration with rapamycin: mechanistic insights

Bové, J., Martínez‐Vicente, M., & Vila, M. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn3068 · Cited by 525 · see citing works

Caspase activation precedes and leads to tangles

de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517 · see citing works

Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders

Sánchez, I., Mahlke, C., & Yuan, J. (2003) · Nature · doi:10.1038/nature01301 · Cited by 504 · see citing works

Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Guerrero-Munoz, M. J., Kiritoshi, T., Neugebauer, V., Jackson, G. R., & Kayed, R. (2012) · Scientific Reports · doi:10.1038/srep00700 · Cited by 502 · see citing works

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485 · see citing works

Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform.

Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441 · see citing works

Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease

Masliah, E., Terry, R. D., DeTeresa, R. M., & Hansen, L. A. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90582-x · Cited by 363 · see citing works

Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease

Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works

Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells

Pickhardt, M., Gažová, Z., von Bergen�, M., Khlistunova, I., Wang, Y., Hascher, A., Mandelkow, E., Biernat, J., & Mandelkow�, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410984200 · Cited by 334 · see citing works

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

Molinari, M., & Helenius, A. (1999) · Nature · doi:10.1038/47062 · Cited by 320 · see citing works

Characterization of Pathology in Transgenic Mice Over-Expressing Human Genomic and cDNA Tau Transgenes

Duff, K., Knight, H., Refolo, L. M., Sanders, S., Yu, X., Picciano, M., Malester, B., Hutton, M. L., Adamson, J., Goedert, M., et al. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0279 · Cited by 311 · see citing works

Changed Conformation of Mutant Tau-P301L Underlies the Moribund Tauopathy, Absent in Progressive, Nonlethal Axonopathy of Tau-4R/2N Transgenic Mice

Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Haesendonck, C. V., Borghgraef, P., & LEUVEN, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409876200 · Cited by 267 · see citing works

Tau truncation during neurofibrillary tangle evolution in Alzheimer’s disease

Guillozet-Bongaarts, A. L., Garcia-Sierra, F., Reynolds, M. R., Horowitz, P. M., Fu, Y., Wang, T., Cahill, M. E., Bigio, E. H., Berry, R. W., & Binder, L. I. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.019 · Cited by 256 · see citing works

Caspase-9 Activation and Caspase Cleavage of tau in the Alzheimer's Disease Brain

Rohn, T. T., Rissman, R. A., Davis, M. C., Kim, Y., Cotman, C. W., & Head, E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0549 · Cited by 242 · see citing works

Soluble forms of tau are toxic in Alzheimer's disease

Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232 · see citing works

Proapoptotic Effects of Tau Cleavage Product Generated by Caspase-3

Chung, C.-W., Song, Y.-H., Kim, I.-K., Yoon, W. J., Ryu, B. R., Jo, D., Woo, H., Kwon, Y.-K., Kim, H., Gwag, B.-J., et al. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0335 · Cited by 211 · see citing works

Assembly of two distinct dimers and higher‐order oligomers from full‐length tau

Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · see citing works

Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability

Flach, K., Hilbrich, I., Schiffmann, A., Gärtner, U., Krüger, M., Leonhardt, M., Waschipky, H., Wick, L., Arendt, T., & Holzer, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396176 · Cited by 188 · see citing works

Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons

Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170 · see citing works

Methylene blue upregulates Nrf2/ARE genes and prevents tau-related neurotoxicity

Stack, C., Jainuddin, S., Elipenahli, C., Gerges, M., Starkova, N. N., Starkov, A. A., Jové, M., Portero‐Otín, M., Launay, N., Pujol, A., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu080 · Cited by 159 · see citing works

Lysosomal Dysfunction Promotes Cleavage and Neurotoxicity of Tau In Vivo

Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001026 · Cited by 148 · see citing works

FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease

Kam, T.-I., Song, S., Gwon, Y., Park, H., Yan, J.-J., Im, I., Choi, J.-W., Choi, T.-Y., Kim, J., Song, D.-K., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66827 · Cited by 128 · see citing works

Cleaved-Tau: A Biomarker of Neuronal Damage after Traumatic Brain Injury

Gabbita, S., Scheff, S., Menard, R. M., Roberts, K. N., Fugaccia, I., & Zemlan, F. (2005) · Journal of Neurotrauma · doi:10.1089/neu.2005.22.83 · Cited by 127 · see citing works

Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated

Hanger, D. P., Brion, J., Gallo, J., Cairns, N. J., Luthert, P. J., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2750099 · Cited by 125 · see citing works

Analysis of Tau Phosphorylation and Truncation in a Mouse Model of Human Tauopathy

Delobel, P., Lavenir, I., Fraser, G. M., Ingram, E., Holzer, M., Ghetti, B. F., Spillantini, M. G., Crowther, R. A., & Goedert, M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070627 · Cited by 120 · see citing works

Methylene Blue Reduced Abnormal Tau Accumulation in P301L Tau Transgenic Mice

Hosokawa, M., Arai, T., Masuda‐Suzukake, M., Nonaka, T., Yamashita, M., Akiyama, H., & Hasegawa, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052389 · Cited by 89 · see citing works

Neuropathogenic role of adenylate kinase-1 in Aβ-mediated tau phosphorylation via AMPK and GSK3β

Park, H., Kam, T., Kim, Y., Choi, H., Gwon, Y., Kim, C., Koh, J., & Jung, Y. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds100 · Cited by 85 · see citing works

Drugs: A tangled web of targets

Gravitz, L. (2011) · Nature · doi:10.1038/475s9a · Cited by 81 · see citing works

Animal models reveal role for tau phosphorylation in human disease

Götz, J., Gladbach, A., Pennanen, L., van Eersel, J., Schild, A., David, D. C., & Ittner, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.008 · Cited by 79 · see citing works

Conformational changes and cleavage of tau in Pick bodies parallel the early processing of tau found in Alzheimer pathology

Mondragón‐Rodríguez, S., Mena, R., Binder, L. I., Smith, M. A., Perry, G. L., & García‐Sierra, F. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2007.00853.x · Cited by 58 · see citing works

Caspase-cleaved tau accumulation in neurodegenerative diseases associated with tau and α-synuclein pathology

Newman, J., Rissman, R. A., Sarsoza, F. M., Kim, R. C., Dick, M. B., Bennett, D. A., Cotman, C. W., Rohn, T. T., & Head, E. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1027-3 · Cited by 55 · see citing works

Truncated tau at D421 is associated with neurodegeneration and tangle formation in the brain of Alzheimer transgenic models

Zhang, Q., Zhang, X., & Sun, A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0491-6 · Cited by 43 · see citing works

Impact of N-tau on adult hippocampal neurogenesis, anxiety, and memory

Pristerà, A., Saraulli, D., Vecchioli, S. F., Strimpakos, G., Costanzi, M., Certo, M. G. D., Cannas, S., Ciotti, M. T., Tirone, F., Mattei, E., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.010 · Cited by 39 · see citing works

Neuronal degeneration, synaptic defects, and behavioral abnormalities in tau45-230 transgenic mice

Lang, A. E., Riherd Methner, D. N., & Ferreira, A. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.06.017 · Cited by 35 · see citing works

Systemic administration of Congo red does not improve motor or cognitive function in R6/2 mice

Wood, N. I., Pallier, P. N., Wanderer, J. P., & Morton, A. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.09.015 · Cited by 31 · see citing works

GSK3β, But Not GSK3α, Inhibits the Neuronal Differentiation of Neural Progenitor Cells As a Downstream Target of Mammalian Target of Rapamycin Complex1

Ahn, J., Jang, J., Choi, J., Lee, J., Oh, S.-H., Lee, J.-H., Yoon, K., & Kim, S. (2014) · Stem Cells and Development · doi:10.1089/scd.2013.0397 · Cited by 29 · see citing works

The promoter of brain-specific angiogenesis inhibitor 1-associated protein 4 drives developmentally targeted transgene expression mainly in adult cerebral cortex and hippocampus

Kim, M., Ahn, K. Y., Lee, S. M., Koh, J. T., Chun, B. J., Bae, C. S., Lee, K. S., & Kim, K. K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.106 · Cited by 13 · see citing works

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works

Synaptic Impairment in Alzheimer’s Disease: A Dysregulated Symphony

Forner, S., Baglietto-Vargas, D., Martini, A. C., Trujillo-Estrada, L., & LaFerla, F. M. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.002 · Cited by 430 · see citing works

Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies

Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works

The role of pathological tau in synaptic dysfunction in Alzheimer’s diseases

Wu, M., Zhang, M., Yin, X., Chen, K., Hu, Z., Zhou, Q., Cao, X., Chen, Z., & Liu, D. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00270-1 · Cited by 241 · see citing works

Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers

Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170 · see citing works

Tau-mediated synaptic and neuronal dysfunction in neurodegenerative disease

Tracy, T. E., & Gan, L. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.04.027 · Cited by 147 · see citing works

Tau localises within mitochondrial sub-compartments and its caspase cleavage affects ER-mitochondria interactions and cellular Ca2+ handling

Cieri, D., Vicario, M., Vallese, F., D’Orsi, B., Berto, P., Grinzato, A., Catoni, C., Stefani, D. D., Rizzuto, R., Brini, M., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.07.011 · Cited by 122 · see citing works

Caspase-3-dependent cleavage of Akt modulates tau phosphorylation via GSK3β kinase: implications for Alzheimer’s disease

Chu, J., Lauretti, E., & Praticò, D. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.214 · Cited by 90 · see citing works

Caspase-Cleaved Tau Impairs Mitochondrial Dynamics in Alzheimer’s Disease

Pérez, M. J., Vergara-Pulgar, K., Jara, C., Cabezas-Opazo, F., & Quintanilla, R. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0385-x · Cited by 81 · see citing works

Potential mechanisms and implications for the formation of tau oligomeric strains

Gerson, J. E., Mudher, A. K., & Kayed, R. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1226251 · Cited by 74 · see citing works

Crosstalk between the mTOR and Nrf2/ARE signaling pathways as a target in the improvement of long-term potentiation

Gureev, A. P., Popov, V. N., & Starkov, A. A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113285 · Cited by 73 · see citing works

Physiological and Pathophysiological Implications of Synaptic Tau

Regan, P. L., Whitcomb, D. J., & Cho, K. (2016) · The Neuroscientist · doi:10.1177/1073858416633439 · Cited by 70 · see citing works

Combining P301L and S320F tau variants produces a novel accelerated model of tauopathy

Koller, E. J., Gonzalez De La Cruz, E., Machula, T., Ibanez, K. R., Lin, W.-L., Williams, T., Riffe, C. J., Ryu, D., Strang, K. H., Liu, X., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz151 · Cited by 63 · see citing works

The Role of Mitochondrial Impairment in Alzheimer´s Disease Neurodegeneration: The Tau Connection

Quntanilla, R. A., & Tapia-Monsalves, C. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200525020259 · Cited by 59 · see citing works

Spermidine/spermine-N1-acetyltransferase ablation impacts tauopathy-induced polyamine stress response

Sandusky‐Beltran, L. A., Kovalenko, A., Ma, C., Calahatian, J. I. T., Placides, D. S., Watler, M., Hunt, J. B., Darling, A. L., Baker, J. D., Blair, L. J., et al. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0507-y · Cited by 51 · see citing works

Caspase-cleaved tau is senescence-associated and induces a toxic gain of function by putting a brake on axonal transport

Conze, C., Rierola, M., Trushina, N. I., Peters, M., Janning, D., Holzer, M., Heinisch, J. J., Arendt, T., Bakota, L., & Brandt, R. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01538-2 · Cited by 50 · see citing works

Differential Hyperphosphorylation of Tau-S199, -T231 and -S396 in Organotypic Brain Slices of Alzheimer Mice. A Model to Study Early Tau Hyperphosphorylation Using Okadaic Acid

Foidl, B. M., & Humpel, C. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00113 · Cited by 47 · see citing works

Characterization of TauC3 antibody and demonstration of its potential to block tau propagation

Nicholls, S. B., DeVos, S. L., Commins, C., Nobuhara, C. K., Bennett, R. E., Corjuc, D. L., Maury, E. A., Eftekharzadeh, B., Akingbade, O., Fan, Z., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177914 · Cited by 45 · see citing works

An update on the association between traumatic brain injury and Alzheimer’s disease: Focus on Tau pathology and synaptic dysfunction

Li, L., Liang, J., & Fu, H. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.10.020 · Cited by 41 · see citing works

Tau Conformation as a Target for Disease-Modifying Therapy: The Role of Truncation

Novák, P., Cehlár, O., Škrabana, R., & Novák, M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179942 · Cited by 36 · see citing works

Small molecule modulation of the p75 neurotrophin receptor inhibits multiple amyloid beta-induced tau pathologies

Yang, T., Tran, K. C., Zeng, A. Y., Massa, S. M., & Longo, F. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-77210-y · Cited by 39 · see citing works

Dendritic/Post-synaptic Tau and Early Pathology of Alzheimer’s Disease

Yin, X., Zhao, C., Qiu, Y., Zhou, Z., Bao, J., & Qian, W. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.671779 · Cited by 39 · see citing works

Tau truncation in the pathogenesis of Alzheimer’s disease: a narrative review

Chu, D., Yang, X., Wang, J., Zhou, Y., Gu, J., Miao, J., Wu, F., & Liu, F. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385853 · Cited by 37 · see citing works

Tau Seeding Mouse Models with Patient Brain-Derived Aggregates

Robert, A., Schöll, M., & Vogels, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116132 · Cited by 35 · see citing works

Carbon dots as dual inhibitors of tau and amyloid-beta aggregation for the treatment of Alzheimer's disease

Zhang, W., Smith, N. S., Zhou, Y., McGee, C. M., Bartoli, M., Fu, S., Chen, J., Domena, J. B., Joji, A., Burr, H., et al. (2024) · Acta Biomaterialia · doi:10.1016/j.actbio.2024.06.001 · Cited by 34 · see citing works

Pimozide reduces toxic forms of tau in TauC3 mice via 5′ adenosine monophosphate‐activated protein kinase‐mediated autophagy

Kim, Y. D., Jeong, E. I., Nah, J., Yoo, S., Lee, W. J., Kim, Y., Moon, S., Hong, S., & Jung, Y. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14109 · Cited by 32 · see citing works

Distinct Mechanisms Underlying Resveratrol-Mediated Protection from Types of Cellular Stress in C6 Glioma Cells

Means, J. C., Gerdes, B. C., & Koulen, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071521 · Cited by 28 · see citing works

Abolishing Tau cleavage by caspases at Aspartate421 causes memory/synaptic plasticity deficits and pre-pathological Tau alterations

Biundo, F., d’Abramo, C., Tambini, M. D., Zhang, H., Prete, D. D., Vitale, F., Giliberto, L., Arancio, O., & D'adamio, L. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.165 · Cited by 24 · see citing works

Heterogeneous Tau Oligomers as Molecular Targets for Alzheimer’s Disease and Related Tauopathies

Lo, C. H. (2022) · Biophysica · doi:10.3390/biophysica2040039 · Cited by 24 · see citing works

Aberrant role of ALK in tau proteinopathy through autophagosomal dysregulation

Park, J., Choi, H., Kim, Y. D., Kim, S.-H., Kim, Y., Gwon, Y., Lee, D. Y., Park, S., Heo, W. D., & Jung, Y. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-01003-y · Cited by 23 · see citing works

Cyclosporine A (CsA) prevents synaptic impairment caused by truncated tau by caspase-3

Tapia-Monsalves, C., Olesen, M. A., Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103861 · Cited by 24 · see citing works

Pathological Impact of Tau Proteolytical Process on Neuronal and Mitochondrial Function: a Crucial Role in Alzheimer’s Disease

Olesen, M. A., & Quintanilla, R. A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03434-4 · Cited by 22 · see citing works

Activity-dependent tau cleavage by caspase-3 promotes neuronal dysfunction and synaptotoxicity

Opland, C. K., Bryan, M. R., Harris, B., McGillion-Moore, J., Tian, X., Chen, Y., Itano, M. S., Diering, G. H., Meeker, R. B., & Cohen, T. J. (2023) · iScience · doi:10.1016/j.isci.2023.106905 · Cited by 21 · see citing works

Tauopathies: Mechanisms and Therapeutic Strategies

Tan, C., Zhang, X.-Y., Tan, L., & Yu, J. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170187 · Cited by 20 · see citing works

Exoenzyme Y induces extracellular active caspase-7 accumulation independent from apoptosis: modulation of transmissible cytotoxicity

Renema, P., Kozhukhar, N., Pastukh, V. V., Spadafora, D., Paudel, S. S., Tambe, D. T., ALEXEYEV, M. F., Frank, D. W., & Stevens, T. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00508.2019 · Cited by 17 · see citing works

Cleavage of human tau at Asp421 inhibits hyperphosphorylated tau induced pathology in a Drosophila model

Chi, H., Lee, S., Shiu, R.-H., Han, R., Hsieh, C.-P., Wei, T.-M., Lo, C., Chang, H.-Y., & Sang, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-70423-1 · Cited by 17 · see citing works

Changes in microtubule-associated protein tau during peripheral nerve injury and regeneration

Yi, S., Zha, G., Shen, M., & Gu, X. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.191227 · Cited by 17 · see citing works

Caspase-6-cleaved Tau fails to induce Tau hyperphosphorylation and aggregation, neurodegeneration, glial inflammation, and cognitive deficits

Noël, A., Foveau, B., & LeBlanc, A. C. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03506-0 · Cited by 16 · see citing works

Targeted proteolytic products of τ and α-synuclein in neurodegeneration

Xia, Y., Lloyd, G. M., & Giasson, B. I. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210028 · Cited by 13 · see citing works

The Role of Caspases in Alzheimer’s Disease: Pathophysiology Implications and Pharmacologic Modulation

Khezri, M. R., & Ghasemnejad-Berenji, M. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220873 · Cited by 12 · see citing works

Accumulation of C-terminal cleaved tau is distinctly associated with cognitive deficits, synaptic plasticity impairment, and neurodegeneration in aged mice

Loon, A. R., Zamudio, F., Sanneh, A., Brown, B., Smeltzer, S., Brownlow, M. L., Quadri, Z., Peters, M. M., Weeber, E. J., Nash, K. R., et al. (2021) · GeroScience · doi:10.1007/s11357-021-00408-z · Cited by 12 · see citing works

Exploring the significance of caspase-cleaved tau in tauopathies and as a complementary pathology to phospho-tau in Alzheimer’s disease: implications for biomarker development and therapeutic targeting

Rizzi, L., & Grinberg, L. T. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01744-9 · Cited by 11 · see citing works

Viral Delivery of Non-Mutated Human Truncated Tau to Neurons Recapitulates Key Features of Human Tauopathy in Wild-Type Mice

Vogels, T., Vargová, G., Brezováková, V., Quint, W. H., & Hromádka, T. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200047 · Cited by 11 · see citing works

Twenty years of therapeutic development in tauopathy mouse models: a scoping review

Langness, V. F., Simmons, D. A., McHugh, T. L. M., Butler, R. R., Zhou, J., Liu, H., Yang, T., Ellerby, L., & Longo, F. M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70578 · Cited by 9 · see citing works

Limitations and Applications of Rodent Models in Tauopathy and Synucleinopathy Research

Szegvari, E., Holec, S. A. M., & Woerman, A. L. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70021 · Cited by 8 · see citing works

Can accelerated ageing models inform us on age‐related tauopathies?

Han, Z. Z., Fleet, A., & Larrieu, D. (2023) · Aging Cell · doi:10.1111/acel.13830 · Cited by 8 · see citing works

Neuronal Expression of Truncated Tau Efficiently Promotes Neurodegeneration in Animal Models: Pitfalls of Toxic Oligomer Analysis

Škrabana, R., Kováčech, B., Filipčík, P., Žilka, N., Jadhav, S., Smolek, T., Kontseková, E., & Novák, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161124 · Cited by 7 · see citing works

iPSC-Induced Neurons with the V337M MAPT Mutation are Selectively Vulnerable to Caspase-Mediated Cleavage of Tau and Apoptotic Cell Death

Theofilas, P., Wang, C., Butler, D., Morales, D. O., Petersen, C., Ambrose, A. J., Chin, B., Yang, T. T. C., Khan, S., Ng, R. A., et al. (2021) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103954 · Cited by 6 · see citing works

Dual truncation of tau by caspase-2 accelerates its CHIP-mediated degradation

Reinhardt, L., Musacchio, F., Bichmann, M., Behrendt, A., Ercan-Herbst, E., Stein, J., Becher, I., Haberkant, P., Mader, J. K., Schöndorf, D. C., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106126 · Cited by 6 · see citing works

Caspase inhibition mitigates tau cleavage and neurotoxicity in iPSC‐induced neurons with the V337M MAPT mutation

Theofilas, P., Ambrose, A. J., Butler, D., Wang, C., Morales, D. O., Petersen, C., Chin, B., Yang, T. T. C., Khan, S., Ng, R. A., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.051471 · Cited by 6 · see citing works

Depletion of TDP-43 exacerbates tauopathy-dependent brain atrophy by sensitizing vulnerable neurons to caspase 3-mediated endoproteolysis of tau in a mouse model of Multiple Etiology DementiaPreprint

Baghel, M. S., Burns, G. D., Tsapatsis, M., Mallika, A. P., Cruz, A. L., Cao, T., Chen, X. K., Rosa, I. D. L., Marx, S. R., Ye, Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.26.600814 · Cited by 6 · see citing works

Telomere-driven senescence accelerates tau pathology, neuroinflammation and neurodegeneration in a tauopathy mouse model

Palomares, D., Vanparys, A., Jorgji, J., Paître, E., Kienlen‐Campard, P., & Suelves, N. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02118-5 · Cited by 7 · see citing works

Sulforaphane prevents cognitive decline and mitochondrial failure induced by hippocampal expression of caspase-3 cleaved tau

Villavicencio-Tejo, F., Olesen, M. A., Ampuero, E., & Quintanilla, R. A. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.105991 · Cited by 5 · see citing works

Astrocytes distress triggers brain pathology through induction of δ secretase in a murine model of Alzheimer’s disease

Schmidt, V., Ziemlińska, E., Obrębski, T., Gomes, J. P., Żurawska-Płaksej, E., Cendrowski, J., Palmfeldt, J., Hempstead, B. L., Willnow, T. E., & Malik, A. R. (2025) · Nature Communications · doi:10.1038/s41467-025-65536-y · Cited by 4 · see citing works

Changes in the Levels of Neurospecific Proteins and Indices of Apoptosis in the Rat Cornea at Chronic Ethanol Consumption: Protective Effects of Thiamine Administration

Pavlova, O., Bilous, V. L., Корса, В. В., Stepanenko, S. P., IuM, P., & Tykhomyrov, A. A. (2022) · Neurophysiology · doi:10.1007/s11062-023-09932-4 · Cited by 4 · see citing works

Tauopathy

Chi, H., Sang, T., & Chang, H.-Y. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.73198 · Cited by 4 · see citing works

Is tau pathology a relevant factor in neuronal damage induced by alcohol and other drugs?

Olesen, M. A., Ancía, A., & Quintanilla, R. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168059 · Cited by 3 · see citing works

The Value of the Object Recognition Paradigm in Investigating Animal Models of Alzheimer's Disease

Mathis, C. (2018) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-12-812012-5.00021-5 · Cited by 3 · see citing works

Molecular Mechanisms of Synaptic Plasticity and Memory and Their Dysfunction in Alzheimer's Disease ☆

Stephens, G. S., You, J. C., Fu, C.-H., & Chin, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.21126-7 · Cited by 1 · see citing works

Alzheimer’s Disease and Frontotemporal Lobar Degeneration: Mouse Models

Ittner, L. M., Lee, W. S., Stefanoska, K., Asih, P. R., & Ke, Y. D. (2018) · Springer eBooks · doi:10.1007/978-3-319-72938-1_10 · Cited by 1 · see citing works

Experimental Models of Tau Aggregation

Buck, K., Jahn, T. R., & Gasparini, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00070-1 · Cited by 1 · see citing works

Aβ-induced distress of astrocytes triggers Alzheimer disease pathology through non-canonical δ secretase activityPreprint

Schmidt, V., Ziemlińska, E., Obrębski, T., Żurawska-Płaksej, E., Cendrowski, J., Hempstead, B. L., Willnow, T. E., & Malik, A. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.30.635618 · Cited by 1 · see citing works

Alzheimer’s Disease and Frontotemporal Lobar Degeneration: Mouse Models

van Eersel, J., Delerue, F., Ittner, L. M., & Ke, Y. D. (2014) · Springer eBooks · doi:10.1007/978-1-4471-6380-0_8

In silico screening of multi-target drugs against Alzheimer's Disease: a repurposing approachPreprint

Amato, M. B., Martinez, D. P., Dias, R. S., Höfs, F. N., & Kremer, F. S. (2024) · Research Square · doi:10.21203/rs.3.rs-4774275/v1

Copy number variations of proteins associated with neurodegenerative diseases and rare neurological disorders

Yang, Z., & Lei, P. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0201

Selective imaging probes for differential detection of pathological tau polymorphs in tauopathies.

Bisi, N., Pinzi, L., & Rastelli, G. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104352

Plasticity of hippocampal synaptic transmission and intrinsic excitability in a mouse model of Alzheimer’s disease

Jiang, N. (2019) · theses.fr (ABES) · doi:10.70675/e788b268zc8e3z491az8d02z52080880e988

Tau Protein in Alzheimer's Disease

Mukherjee, M., Dhara, S., Jana, A., & Roy, T. (2026) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9798898815646126010005

Tau physiology and pathology: impacts on cellular structures and neurodegenerative diseases

Akbari, V., & Bahramikia, S. (2026) · InflammoPharmacology · doi:10.1007/s10787-026-02328-w

Cell-Based Tau Polymerization Assays

Horgan, N. G., Ibrahium, O. M. H., Ademoye, T. A., Fortin, J. S., & Ostafe, R. (2026) · Neuromethods · doi:10.1007/978-1-0716-5234-3_12

New Insight into Alzheimer’s Disease via Caspase 3-cleaved Tau: Pathogenic Role in Tau Oligomer Formation and Memory Deficits

Kima, Y. D., Parka, J., & Jung, Y. (2017) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000344 · Cited by 2 · see citing works

P1‐159: Truncated tau transgenic mice model showing memory impairment in early age

Kim, Y. D., Choi, H. W., Park, H., & Jung, Y. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.709

Caspase-3-Dependent Proteolytic Cleavage of Tau Causes Neurofibrillary Tangles and Results in Cognitive Impairment During Normal Aging

Means, J. C., Gerdes, B. C., Kaja, S., Sumien, N., Payne, A. J., Stark, D. A., Borden, P. K., Price, J. L., & Koulen, P. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1942-9 · Cited by 54 · see citing works

Preventing Pathology in a Transgenic Mouse Model of Alzheimer's Disease Following Over-Expression of BCL-2

Vyas, V. (2007) · ScholarWorks (Boise State University)

P1‐361: Extracellular oligomeric tau inhibits memory formation in mice

Moe, J. G., Chatterjee, I., Puzzo, D., Staniszewski, A., Fà, M., Davidowitz, E. J., & Arancio, O. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.915 · Cited by 5 · see citing works